ID PYRC_ACIAD Reviewed; 344 AA. AC Q6FD29; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 122. DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219}; DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219}; DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219}; GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219}; GN OrderedLocusNames=ACIAD1150; OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Moraxellales; Moraxellaceae; Acinetobacter. OX NCBI_TaxID=62977; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33305 / BD413 / ADP1; RX PubMed=15514110; DOI=10.1093/nar/gkh910; RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.; RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, RT a versatile and naturally transformation competent bacterium."; RL Nucleic Acids Res. 32:5766-5779(2004). CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate + H(+); CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00219}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00219}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP- CC Rule:MF_00219}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC DHOase family. Class II DHOase subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00219}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR543861; CAG68030.1; -; Genomic_DNA. DR RefSeq; WP_004921413.1; NC_005966.1. DR AlphaFoldDB; Q6FD29; -. DR SMR; Q6FD29; -. DR STRING; 202950.GCA_001485005_01220; -. DR MEROPS; M38.A02; -. DR GeneID; 45233583; -. DR KEGG; aci:ACIAD1150; -. DR eggNOG; COG0418; Bacteria. DR HOGENOM; CLU_041558_1_0_6; -. DR OrthoDB; 9808095at2; -. DR BioCyc; ASP62977:ACIAD_RS05295-MONOMER; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000430; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:TreeGrafter. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd01294; DHOase; 1. DR FunFam; 3.20.20.140:FF:000006; Dihydroorotase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR HAMAP; MF_00219; PyrC_classII; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR004721; DHOdimr. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR00856; pyrC_dimer; 1. DR PANTHER; PTHR43137; DIHYDROOROTASE; 1. DR PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR PIRSF; PIRSF001237; DHOdimr; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome; KW Zinc. FT CHAIN 1..344 FT /note="Dihydroorotase" FT /id="PRO_1000024007" FT ACT_SITE 247 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 15..17 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 41 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 219 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT BINDING 263 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" FT MOD_RES 99 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219" SQ SEQUENCE 344 AA; 38867 MW; DE11304473479E6E CRC64; MDTITLLQPD DWHAHLRDGL ALKRTVPDLA QQFARAICMP NLVPPVKTVD EAEAYRERIM AHVPEGVHFD PRMVLYFTDH TSPSEVKKIK DSAHVNAIKL YPAGATTNSD NGVSDIRKVY AVIEQLEEHQ VPLLLHGEVT HHHVDIFDRE KRFLDEVLSP LLKQFPKLKL VLEHITTSEA AHFVLEQDRN VAATITPQHL LFNRNDMLVG GIKPHFYCLP ILKRQTHQQT LIEVATSGNP KFFLGTDSAP HSKNAKENAC GCAGCYSAPT AIELYAQAFD QVNKIERLEG FASHFGADFY GLPRNTNTIT LVKEDQIIPE QLDYLDDEKI IPLYAGKTIQ WRKV //